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Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents

Lipases have key roles in insect lipid acquisition, storage, and mobilization and are also fundamental to many physiological processes in insects. Lipids are an important component of insect diets, where they are hydrolyzed in the midgut lumen, absorbed, and used for the synthesis of complex lipids....

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Autores principales: Santana, Camilla Camerino, Barbosa, Leandro A., Diniz Basílio Júnior, Irinaldo, Gomes do Nascimento, Ticiano, Dornelas, Camila Braga, Grillo, Luciano A.M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620720/
https://www.ncbi.nlm.nih.gov/pubmed/28902170
http://dx.doi.org/10.3390/insects8030100
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author Santana, Camilla Camerino
Barbosa, Leandro A.
Diniz Basílio Júnior, Irinaldo
Gomes do Nascimento, Ticiano
Dornelas, Camila Braga
Grillo, Luciano A.M.
author_facet Santana, Camilla Camerino
Barbosa, Leandro A.
Diniz Basílio Júnior, Irinaldo
Gomes do Nascimento, Ticiano
Dornelas, Camila Braga
Grillo, Luciano A.M.
author_sort Santana, Camilla Camerino
collection PubMed
description Lipases have key roles in insect lipid acquisition, storage, and mobilization and are also fundamental to many physiological processes in insects. Lipids are an important component of insect diets, where they are hydrolyzed in the midgut lumen, absorbed, and used for the synthesis of complex lipids. The South American palm weevil Rhynchophorus palmarum is one of the most important pests on commercial palm plantations. However, there are few studies about lipid digestion for this insect. In this work, we have described the biochemical characterization of the lipase activity in the posterior midgut of the R. palmarum palm weevil. Lipase activity was highest between the temperatures of 37 °C and 45 °C and at pH 6.5. Lipase activity was also sensitive to variations in salt and calcium concentrations. Lipases have been described structurally as enzymes with the Ser-His-Asp Catalytic Triad, containing an active serine. The serine protease inhibitor PMSF (phenylmethane sulfonyl fluoride) inhibited the lipases from R. palmarum, demonstrating the importance of a serine residue for this activity. The ability of the lipases to hydrolyze p-Nitrophenyl esters with different chain lengths has revealed the activities of a broad range of substrates. The lipase activities of R. palmarum increased in the presence of reduced glutathione (GSH) and dithiothreitol (DTT), while in the presence of oxidized glutathione (GSSG), activities were drastically reduced. To our knowledge, this study has provided the first information about lipase activity in the R. palmarum palm weevil.
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spelling pubmed-56207202017-10-03 Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents Santana, Camilla Camerino Barbosa, Leandro A. Diniz Basílio Júnior, Irinaldo Gomes do Nascimento, Ticiano Dornelas, Camila Braga Grillo, Luciano A.M. Insects Article Lipases have key roles in insect lipid acquisition, storage, and mobilization and are also fundamental to many physiological processes in insects. Lipids are an important component of insect diets, where they are hydrolyzed in the midgut lumen, absorbed, and used for the synthesis of complex lipids. The South American palm weevil Rhynchophorus palmarum is one of the most important pests on commercial palm plantations. However, there are few studies about lipid digestion for this insect. In this work, we have described the biochemical characterization of the lipase activity in the posterior midgut of the R. palmarum palm weevil. Lipase activity was highest between the temperatures of 37 °C and 45 °C and at pH 6.5. Lipase activity was also sensitive to variations in salt and calcium concentrations. Lipases have been described structurally as enzymes with the Ser-His-Asp Catalytic Triad, containing an active serine. The serine protease inhibitor PMSF (phenylmethane sulfonyl fluoride) inhibited the lipases from R. palmarum, demonstrating the importance of a serine residue for this activity. The ability of the lipases to hydrolyze p-Nitrophenyl esters with different chain lengths has revealed the activities of a broad range of substrates. The lipase activities of R. palmarum increased in the presence of reduced glutathione (GSH) and dithiothreitol (DTT), while in the presence of oxidized glutathione (GSSG), activities were drastically reduced. To our knowledge, this study has provided the first information about lipase activity in the R. palmarum palm weevil. MDPI 2017-09-13 /pmc/articles/PMC5620720/ /pubmed/28902170 http://dx.doi.org/10.3390/insects8030100 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Santana, Camilla Camerino
Barbosa, Leandro A.
Diniz Basílio Júnior, Irinaldo
Gomes do Nascimento, Ticiano
Dornelas, Camila Braga
Grillo, Luciano A.M.
Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents
title Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents
title_full Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents
title_fullStr Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents
title_full_unstemmed Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents
title_short Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents
title_sort lipase activity in the larval midgut of rhynchophorus palmarum: biochemical characterization and the effects of reducing agents
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620720/
https://www.ncbi.nlm.nih.gov/pubmed/28902170
http://dx.doi.org/10.3390/insects8030100
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